Author Correction: Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover

Corrections &amendments Author Correction: Structural dynamics of the midnolinproteasome during ubiquitin-independent substrate turnover Correction to: Nature Communications https://doi.org/10.1038/s41467-026-71002-0, published online 27 March 2026 Chuanda Zhu , Lu Qin, Zonglin Dai , Peng Zuo , Ao Yang, Lijun Zhong, Zhiqiang Lin & Ling Liang https://doi.org/10.1038/s41467-026-74286-4 Following publication, some text has been updated for clarity. In the abstract, “Our structures reveal that midnolin binds to the proteasome via the RPN1 subunit by its C-terminal helix, and its ubiquitin-like domain interacts with the RPN11 deubiquitinase in a non-catalytic role” now replaces the original “Our structures reveal that midnolin binds to the proteasome via the RPN1 subunit by its C-terminal helix. Unexpectedly, its ubiquitin-like domain interacts with the RPN11 deubiquitinase in a non-catalytic role.” In the second paragraph, “The Ubl domain of midnolin is essential for degradation activity. However, unlike canonical shuttle factors such as Rad23 and ubiquilins, which use their Ubl domains to bind the proteasome, the midnolin Ubl domain is dispensable for proteasome and substrate binding” now replaces “Paradoxically, the Ubl domain, which is essential for degradation activity, is dispensable for substrate and proteasome binding.” In the first paragraph of the “The αHelix-C of midnolin interacts with RPN1 (PSMD2) dynamically” section, “Our cryo-EM analysis is consistent with previous studies12,13,” now replaces the original “Our cryo-EM analysis revealed that different from previous studies, ….” The text is updated in the HTML and PDF versions of the article. 1234567890():,; 1234567890():,; Check for updates Open Access This article is licensed under a Creative Commons Attribution-NonCommercialNoDerivatives 4.0 International License, which permits any non-commercial use, sharing, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/. © The Author(s) 2026 nature communications (2026)17:5214 | 1  (...truncated)